Evidence map›Paper›PMID 38758395›Full record

ArticleCellular and molecular life sciences : CMLS2024

Autophagy initiation triggers p150

Aleksandra Tempes, Karolina Bogusz, Agnieszka Brzozowska, Jan Weslawski, Matylda Macias, Oliver Tkaczyk, Katarzyna Orzoł, Aleksandra Lew, Malgorzata Calka-Kresa, Tytus Bernas and 9 more

Abstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

19 authors.

Aleksandra Tempes *Laboratory of Molecular and Cellular Neurobiology, International Institute of Molecular and Cell Biology, Ks. Trojdena St. 4, 02-109, Warsaw, Poland.
Karolina Bogusz *Laboratory of Molecular and Cellular Neurobiology, International Institute of Molecular and Cell Biology, Ks. Trojdena St. 4, 02-109, Warsaw, Poland.
Agnieszka Brzozowska *Laboratory of Molecular and Cellular Neurobiology, International Institute of Molecular and Cell Biology, Ks. Trojdena St. 4, 02-109, Warsaw, Poland.
Jan Weslawski *Laboratory of Molecular and Cellular Neurobiology, International Institute of Molecular and Cell Biology, Ks. Trojdena St. 4, 02-109, Warsaw, Poland.
Matylda MaciasMicroscopy and Flow Cytometry Core Facility, International Institute of Molecular and Cell Biology, Warsaw, Poland.
Oliver TkaczykLaboratory of Molecular and Cellular Neurobiology, International Institute of Molecular and Cell Biology, Ks. Trojdena St. 4, 02-109, Warsaw, Poland.
Katarzyna OrzołLaboratory of Molecular and Cellular Neurobiology, International Institute of Molecular and Cell Biology, Ks. Trojdena St. 4, 02-109, Warsaw, Poland.
Aleksandra LewLaboratory of Molecular and Cellular Neurobiology, International Institute of Molecular and Cell Biology, Ks. Trojdena St. 4, 02-109, Warsaw, Poland.
Malgorzata Calka-KresaNencki Institute of Experimental Biology, Polish Academy of Sciences, Warsaw, Poland.
Tytus BernasNencki Institute of Experimental Biology, Polish Academy of Sciences, Warsaw, Poland.
Andrzej A SzczepankiewiczNencki Institute of Experimental Biology, Polish Academy of Sciences, Warsaw, Poland.
Magdalena MlostekLaboratory of Molecular and Cellular Neurobiology, International Institute of Molecular and Cell Biology, Ks. Trojdena St. 4, 02-109, Warsaw, Poland.
Shiwani KumariLaboratory of Molecular and Cellular Neurobiology, International Institute of Molecular and Cell Biology, Ks. Trojdena St. 4, 02-109, Warsaw, Poland.
Ewa LiszewskaLaboratory of Molecular and Cellular Neurobiology, International Institute of Molecular and Cell Biology, Ks. Trojdena St. 4, 02-109, Warsaw, Poland.
Katarzyna MachnickaLaboratory of Molecular and Cellular Neurobiology, International Institute of Molecular and Cell Biology, Ks. Trojdena St. 4, 02-109, Warsaw, Poland.
Magdalena BakunInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
Tymon RubelInstitute of Radioelectronics and Multimedia Technology, Warsaw University of Technology, Warsaw, Poland.
Anna R MalikLaboratory of Molecular and Cellular Neurobiology, International Institute of Molecular and Cell Biology, Ks. Trojdena St. 4, 02-109, Warsaw, Poland. ar.malik@uw.edu.pl.ORCID http://orcid.org/0000-0001-7732-0756
Jacek JaworskiLaboratory of Molecular and Cellular Neurobiology, International Institute of Molecular and Cell Biology, Ks. Trojdena St. 4, 02-109, Warsaw, Poland. jaworski@iimcb.gov.pl.ORCID http://orcid.org/0000-0001-8760-7865

Funding

Fundacja na rzecz Nauki Polskiej POMOST/2013-7/10Fundacja na rzecz Nauki Polskiej TEAM_POIR.04.04.00-00-5CBE/17-00Ministerstwo Edukacji i Nauki I.3.4 Action of the Excellence Initiative - Research University Programme at the University of WarsawNarodowe Centrum Nauki 2016/21/B/NZ3/03639Narodowe Centrum Nauki 2017/25/N/NZ3/01280Narodowe Centrum Nauki 2017/27/B/NZ3/01358
6 · The paper itself

Abstract

The endocytic adaptor protein 2 (AP-2) complex binds dynactin as part of its noncanonical function, which is necessary for dynein-driven autophagosome transport along microtubules in neuronal axons. The absence of this AP-2-dependent transport causes neuronal morphology simplification and neurodegeneration. The mechanisms that lead to formation of the AP-2-dynactin complex have not been studied to date. However, the inhibition of mammalian/mechanistic target of rapamycin complex 1 (mTORC1) enhances the transport of newly formed autophagosomes by influencing the biogenesis and protein interactions of Rab-interacting lysosomal protein (RILP), another dynein cargo adaptor. We tested effects of mTORC1 inhibition on interactions between the AP-2 and dynactin complexes, with a focus on their two essential subunits, AP-2β and p150

Indexed as

AutophagyDynactin ComplexLysosomesAdaptor Protein Complex 2AnimalsAutophagosomesHumansLysosomal-Associated Membrane Protein 1Mechanistic Target of Rapamycin Complex 1MiceNeuronsProtein BindingSirolimusAdaptor Protein Complex 2Dynactin ComplexLysosomal-Associated Membrane Protein 1Mechanistic Target of Rapamycin Complex 1SirolimusAP-2 adaptor complexAutophagyDynactinLysosomesmTORC1p150Glued

Identifiers

PMID38758395
PMCPMC11101406

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.